Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 14, Issue 2, Pages 211-215Publisher
SPRINGER
DOI: 10.1007/s12104-020-09947-6
Keywords
High potential iron-sulfur proteins; Metalloproteins; Paramagnetic NMR; Fast nuclear relaxation
Categories
Funding
- European EC [810856, 4509]
- COST (European Cooperation in Science and Technology) [CA15133]
- Fondazione Ente Cassa di Risparmio di Firenze [CRF 2016 0985]
- FEDER Funds through COMPETE2020Programa Operacional Competitividade e Internacionalizacao (POCI), Fundacao para a Ciencia e a Tecnologia (FCT) Portugal [LISBOA-01-0145-FEDER-007660, PD/BD/135187/2017]
- Fundação para a Ciência e a Tecnologia [PD/BD/135187/2017] Funding Source: FCT
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High potential iron-sulfur proteins (HiPIPs) are a class of small proteins (50-100 aa residues), containing a 4Fe-4S iron-sulfur cluster. The 4Fe-4S cluster shuttles between the oxidation states [Fe4S4](3+/2+), with a positive redox potential in the range (500-50 mV) throughout the different known HiPIPs. Both oxidation states are paramagnetic at room temperature. HiPIPs are electron transfer proteins, isolated from photosynthetic bacteria and usually provide electrons to the photosynthetic reaction-center. PioC, the HIPIP isolated from Rhodopseudomonas palustris TIE-1, is the smallest among all known HiPIPs. Despite their small dimensions, an extensive NMR assignment is only available for two of them, because paramagnetism prevents the straightforward assignment of all resonances. We report here the complete NMR assignment of H-1, C-13 and N-15 signals for the reduced [Fe4S4](2+) state of the protein. A set of double and triple resonance experiments performed with standardized parameters/datasets provided the assignment of about 72% of the residues. The almost complete resonance assignment (99.5% of backbone and ca. 90% of side chain resonances) was achieved by combining the above information with those obtained using a second set of NMR experiments, in which acquisition and processing parameters, as well as pulse sequences design, were optimized to account for the peculiar features of this paramagnetic protein.
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